Protein control of nucleic acid transcription and translation is basic to all life, but the detailed chemical mechanisms for recognition, binding, and control are poorly understood. A series of experiments is described to study the structure of a translational activating protein, COM, as cloned from bacteriophage Mu, and to study its interactions with its cognate nucleic acid. COM offers a simple paradigm for such proteins. It is a small (62 amino acids), single domain, zinc finger protein. Specific structural studies are proposed for COM using 1D and 2D NMR and EXAFS spectroscopies. the holoprotein structure metal binding and RNA binding will be compared with that of the isolated Zn binding peptide (34 amino acids). Finally, fluorescence energy transfer studies will be used to help define the three-dimensional structure of the COM nucleic acid adduct. Taken together these studies may provide key data on the structure of a translational activating protein and provide the primary data on the mechanisms by which it recognizes, binds, and alters translation of its cognate RNA.